원문정보
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초록
영어
Cyclic AMP receptor protein(CRP) is involved in the activation of many genes corresponding to catabolite enzymes in Escherichia coli. In this study, mutant CRP(S128A) was used to elucidate the effect of Ser 128 on the cAMP-induced structural change. Based on the protease digestion and thermal analysis, serine 128 in CRP affects the cAMP binding capability and then structural change of CRP protein. In addition, CD spectra in near UV region revealed that S128A CRP retained the sensitive conformation to thermal effect relative to that of wild-type CRP, in spite of identical Tm values in the absence of cAMP.
목차
Abstract
1. Introduction
2. Materials and Methods
2.1. Protein Purification
2.2. Proteolytic Digestion
2.3. Circular Dichroism Measurement
3. Results and Discussion
4. Conclusion
References
1. Introduction
2. Materials and Methods
2.1. Protein Purification
2.2. Proteolytic Digestion
2.3. Circular Dichroism Measurement
3. Results and Discussion
4. Conclusion
References
저자정보
참고문헌
자료제공 : 네이버학술정보